Lipoprotein lipase (LPL) is functionally active only as a dimer. It is
also generally assumed that the highly homologous hepatic lipase functions
as a dimer, but no clear evidence has been presented. A hepatic
lipase-like activity, also indicated as L-type lipase, is present in
adrenal and ovary tissues. This enzyme is thought to originate from the
liver and to be identical to hepatic lipase. We determined the functional
molecular mass of hepatic lipase in rat liver, adrenal gland and ovary by
radiation inactivation, a method for determining the functional size of a
protein without the need of prior purification. Samples were exposed to
ionizing radiation at -135 degrees C. Hepatic lipase activity in liver
homogenate showed a single exponential decay. The functional molecular
mass was calculated to be 63 +/- 10 kDa. Hepatic lipase activity in
adrenal homogenate was found to have a functional molecular mass of 117
+/- 16 kDa. The functional molecular masses of the lipases partially
purified from rat liver perfusate, adrenal homogenate or ovarian
homogenate showed the same pattern, a target mass for the liver enzyme of
56 +/- 6 kDa and a target mass of 117 +/- 14 kDa for the enzyme from
adrenal gland or ovary. In Western blot analysis the mass of the
structural units of hepatic lipase in liver was 57 kDa and in adrenal and
ovary tissue 51 kDa. We conclude that the functional unit of hepatic
lipase in the liver is a monomer. The enzyme in adrenal gland and ovary is
different from the liver and the functional unit may be a dimer
